Free energy landscapes for initiation and branching of protein aggregation
Identifieur interne : 000350 ( Main/Merge ); précédent : 000349; suivant : 000351Free energy landscapes for initiation and branching of protein aggregation
Auteurs : Weihua Zheng ; Nicholas P. Schafer ; Peter G. WolynesSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2013.
Abstract
This study leverages a predictive protein-folding simulation model to study the free energy landscapes of fused oligomeric constructs to quantify the conditions under which these constructs spontaneously misfold. Constructs of this type have been used to probe the early stages of aggregation in the laboratory. Oligomeric species may be the toxic agents in misfolding-related diseases. The critical structures that initiate aggregation are shown to depend on specific sequence signals and thermodynamic conditions. Our results also suggest that branching due to the presence of multiple amyloidogenic segments may determine the morphology of protein aggregates.
Url:
DOI: 10.1073/pnas.1320483110
PubMed: 24284165
PubMed Central: 3870682
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PMC:3870682Le document en format XML
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<front><div type="abstract" xml:lang="en"><title>Significance</title>
<p>This study leverages a predictive protein-folding simulation model to study the free energy landscapes of fused oligomeric constructs to quantify the conditions under which these constructs spontaneously misfold. Constructs of this type have been used to probe the early stages of aggregation in the laboratory. Oligomeric species may be the toxic agents in misfolding-related diseases. The critical structures that initiate aggregation are shown to depend on specific sequence signals and thermodynamic conditions. Our results also suggest that branching due to the presence of multiple amyloidogenic segments may determine the morphology of protein aggregates.</p>
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